Structure of PDB 7z15 Chain G

Receptor sequence
>7z15G (length=353) Species: 562 (Escherichia coli) [Search protein sequence]
MYVAVKGGEKAIDAAHALQESRRRGDTDLPELSVAQIEQQLNLAVDRVMT
EGGIADRELAALALKQASGDNVEAIFLLRAYRTTLAKLAVSEPLDTTGMR
LERRISAVYKDIPGGQLLGPTYDYTHRLLDFTLLANGEAPTLTTADSEQQ
PSPHVFSLLARQGLAKFEEDSGAQPDDITRTPPVYPCSRSSRLQQLMRGD
EGYLLALAYSTQRGYGRNHPFAGEIRSGYIDVSIVPEELGFAVNVGELLM
TECEMVNGFIDPPDEPPHFTRGYGLVFGMSERKAMAMALVDRALQAPEYG
EHATGPAQDEEFVLAHADNVEAAGFVSHLKLPHYVDFQAELELLKRLQQE
KNH
3D structure
PDB7z15 Structural remodelling of the carbon-phosphorus lyase machinery by a dual ABC ATPase.
ChainG
Resolution1.93 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.7.8.37: alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 ZN G H328 H333 H328 H333
BS02 I9X G H328 H333 H328 H333
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0016740 transferase activity
GO:0061693 alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase activity
Biological Process
GO:0015716 organic phosphonate transport
GO:0019634 organic phosphonate metabolic process
GO:0019700 organic phosphonate catabolic process
Cellular Component
GO:0061694 alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase complex
GO:1904176 carbon phosphorus lyase complex

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:7z15, PDBe:7z15, PDBj:7z15
PDBsum7z15
PubMed36813778
UniProtP16687|PHNI_ECOLI Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnI (Gene Name=phnI)

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